메뉴 건너뛰기




Volumn 31, Issue 4, 1998, Pages 317-323

Activation of tau protein kinase I/glycogen synthase kinase-3β by amyloid β peptide (25-35) enhances phosphorylation of tau in hippocampal neurons

Author keywords

Amyloid protein; Hippocampal culture; Phosphorylation; Tau; TPK I GSK 3

Indexed keywords

ANTIBODY; ANTISENSE OLIGONUCLEOTIDE; GLYCOGEN SYNTHASE; MITOGEN ACTIVATED PROTEIN KINASE; PEPTIDE FRAGMENT; PROTEIN KINASE; TAU PROTEIN;

EID: 0031695652     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-0102(98)00061-3     Document Type: Article
Times cited : (277)

References (35)
  • 1
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • Alonso A.C., Zaidi T., Grundke-Iqbal I., Iqbal K. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc. Natl. Acad. Sci. USA. 91:1994;5562-5566.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5562-5566
    • Alonso, A.C.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 2
    • 0027338266 scopus 로고
    • Phosphorylation of serine 262 strongly reduces the binding of tau protein to microtubules: Distinction between PHF-like immunoreactivity and microtubule-binding
    • Biernat J., Gustke N., Drewes G., Mandelkow E.-M., Mandelkow E. Phosphorylation of serine 262 strongly reduces the binding of tau protein to microtubules: distinction between PHF-like immunoreactivity and microtubule-binding. Neuron. 11:1993;153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 3
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder L.I., Frankfurter A., Rebhun L.I. The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101:1985;1371-1378.
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 4
    • 0027429479 scopus 로고
    • Developmental changes in tau phosphorylation: Fetal-type tau is transiently phosphorylated in a manner similar to paired helical filament-tau characteristic of Alzheimer's disease
    • Brion J.P., Smith C., Couck A.M., Gallo J.M., Anderton B.H. Developmental changes in tau phosphorylation: fetal-type tau is transiently phosphorylated in a manner similar to paired helical filament-tau characteristic of Alzheimer's disease. J. Neurochem. 61:1993;2071-2080.
    • (1993) J. Neurochem. , vol.61 , pp. 2071-2080
    • Brion, J.P.1    Smith, C.2    Couck, A.M.3    Gallo, J.M.4    Anderton, B.H.5
  • 5
    • 0028986916 scopus 로고
    • Amyloid Fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., Yankner B.A. Amyloid Fibrils induce tau phosphorylation and loss of microtubule binding. Neuron. 14:1995;879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 6
    • 0026625670 scopus 로고
    • Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain
    • Correas I., Diaz-Nido J., Avila J. Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain. J. Biol. Chem. 267:1992;15721-15728.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15721-15728
    • Correas, I.1    Diaz-Nido, J.2    Avila, J.3
  • 7
    • 0026549985 scopus 로고
    • Mitogen-activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state
    • Drewes G., Lichtenberg-Kraag B., Doring F. et al. Mitogen-activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state. EMBO J. 11:1992;2131-2138.
    • (1992) EMBO J. , vol.11 , pp. 2131-2138
    • Drewes, G.1    Lichtenberg-Kraag, B.2    Doring, F.3
  • 8
    • 0022896901 scopus 로고
    • Tau function in living cells
    • Drubin D.G., Kirschner M.W. Tau function in living cells. J. Cell Biol. 103:1986;2739-2746.
    • (1986) J. Cell Biol. , vol.103 , pp. 2739-2746
    • Drubin, D.G.1    Kirschner, M.W.2
  • 9
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein-tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A. Multiple isoforms of human microtubule-associated protein-tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron. 3:1989;519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 12
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy J.A., aand Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science. 256:1992;184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Aand Higgins, G.A.2
  • 13
    • 0022724941 scopus 로고
    • Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease
    • Ihara Y., Nukina N., Miura R., Ogawara M. Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease. J. Biochem. 99:1986;1807-1810.
    • (1986) J. Biochem , vol.99 , pp. 1807-1810
    • Ihara, Y.1    Nukina, N.2    Miura, R.3    Ogawara, M.4
  • 14
    • 0025856776 scopus 로고
    • A serine/threonine proline kinase activity is included inthe tau protein kinase fraction forming a paired helical filament epitope
    • Ishiguro K., Omori A., Sato K., Tomizawa K., Imahori K., Uchida T. A serine/threonine proline kinase activity is included inthe tau protein kinase fraction forming a paired helical filament epitope. Neurosci. Lett. 128:1991;195-198.
    • (1991) Neurosci. Lett. , vol.128 , pp. 195-198
    • Ishiguro, K.1    Omori, A.2    Sato, K.3    Tomizawa, K.4    Imahori, K.5    Uchida, T.6
  • 15
    • 0026619472 scopus 로고
    • Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments
    • Ishiguro K., Omori A., Takamatsu M., Sato K., Arioka M., Uchida T., Imahori K. Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments. Neurosci. Lett. 148:1992;202-206.
    • (1992) Neurosci. Lett. , vol.148 , pp. 202-206
    • Ishiguro, K.1    Omori, A.2    Takamatsu, M.3    Sato, K.4    Arioka, M.5    Uchida, T.6    Imahori, K.7
  • 16
    • 0027255817 scopus 로고
    • Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments
    • Ishiguro K., Shiratsuchi A., Sato S. et al. Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments. FEBS Lett. 325:1993;167-172.
    • (1993) FEBS Lett. , vol.325 , pp. 167-172
    • Ishiguro, K.1    Shiratsuchi, A.2    Sato, S.3
  • 17
    • 0029618170 scopus 로고
    • Analysis of phosphorylation of tau with antibodies specific for phosphorylation sites
    • Ishiguro K., Sato K., Takamatsu M., Park J., Uchida T., Imahori K. Analysis of phosphorylation of tau with antibodies specific for phosphorylation sites. Neurosci. Lett. 202:1995;81-84.
    • (1995) Neurosci. Lett. , vol.202 , pp. 81-84
    • Ishiguro, K.1    Sato, K.2    Takamatsu, M.3    Park, J.4    Uchida, T.5    Imahori, K.6
  • 18
    • 0024438227 scopus 로고
    • Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA
    • Kanai Y., Takemura R., Oshima T. et al. Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA. J. Cell Biol. 109:1989;1173-1184.
    • (1989) J. Cell Biol. , vol.109 , pp. 1173-1184
    • Kanai, Y.1    Takemura, R.2    Oshima, T.3
  • 19
    • 0026711059 scopus 로고
    • Fetal-type phosphorylation of the tau in paired helical filaments
    • Kanemaru K., Takio K., Miura R., Titani K., Ihara Y. Fetal-type phosphorylation of the tau in paired helical filaments. J. Neurochem. 58:1992;1667-1675.
    • (1992) J. Neurochem. , vol.58 , pp. 1667-1675
    • Kanemaru, K.1    Takio, K.2    Miura, R.3    Titani, K.4    Ihara, Y.5
  • 20
    • 0027372016 scopus 로고
    • The extent of phosphorylation of fetal tau is comparable to that of PHF-tau from Alzheimer paired helical filaments
    • Kenessey A., Yen S.-H.C. The extent of phosphorylation of fetal tau is comparable to that of PHF-tau from Alzheimer paired helical filaments. Brain Res. 629:1993;40-46.
    • (1993) Brain Res. , vol.629 , pp. 40-46
    • Kenessey, A.1    Yen, S.-H.C.2
  • 21
    • 0023434104 scopus 로고
    • MAP2 and tau segregate into dendritic and axonal domains after the elaboration of morphologically distinct neurites: An immunocytochemical study of cultured rat cerebrum
    • Kosik K.S., Finch E.A. MAP2 and tau segregate into dendritic and axonal domains after the elaboration of morphologically distinct neurites: an immunocytochemical study of cultured rat cerebrum. J. Neurosci. 7:1987;3142-3153.
    • (1987) J. Neurosci. , vol.7 , pp. 3142-3153
    • Kosik, K.S.1    Finch, E.A.2
  • 22
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee V.M.-Y., Balin B.J., Otvos L., Trojanowski J.Q. A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science. 251:1991;675-678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.-Y.1    Balin, B.J.2    Otvos, L.3    Trojanowski, J.Q.4
  • 23
    • 0027522969 scopus 로고
    • A specific immunoprecipitation assay for the protein kinase FA/ glycogen synthase kinase 3
    • Lint J.V., Khandelwal R.L., Merlevede W., Vandenheede J.R. A specific immunoprecipitation assay for the protein kinase FA/ glycogen synthase kinase 3. Anal. Biochem. 208:1993;132-137.
    • (1993) Anal. Biochem. , vol.208 , pp. 132-137
    • Lint, J.V.1    Khandelwal, R.L.2    Merlevede, W.3    Vandenheede, J.R.4
  • 24
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo E.S., Shin R.-W., Billingsley M.L., Van de Voorde A., O'Connor M., Trojanowski J.Q., Lee V.M.-Y. Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron. 13:1994;989-1002.
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.-W.2    Billingsley, M.L.3    Van De Voorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.-Y.7
  • 25
    • 0026570528 scopus 로고
    • Amyloid peptides destabilize calcium homeostasisand render human cortical neurons volunerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R.E. Amyloid peptides destabilize calcium homeostasisand render human cortical neurons volunerable to excitotoxicity. J. Neurosci. 12:1992;376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 27
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D.J. The molecular pathology of Alzheimer's disease. Neuron. 6:1991;487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 28
    • 0028933292 scopus 로고
    • Involvement of tau protein kinase I in paired helical filament-like phosphorylation of the juvenile tau in rat brain
    • Takahashi M., Tomizawa K., Kato R., Sato K., Uchida T., Fujita S.C., Imahori K. Involvement of tau protein kinase I in paired helical filament-like phosphorylation of the juvenile tau in rat brain. J. Neurochem. 64:1994;1759-1768.
    • (1994) J. Neurochem. , vol.64 , pp. 1759-1768
    • Takahashi, M.1    Tomizawa, K.2    Kato, R.3    Sato, K.4    Uchida, T.5    Fujita, S.C.6    Imahori, K.7
  • 29
    • 0027240081 scopus 로고
    • Tau protein kinase I is essential for amyloid β-protein-induced neurotoxicity
    • Takashima A., Noguchi K., Hoshino T., Imahori K. Tau protein kinase I is essential for amyloid β-protein-induced neurotoxicity. Proc. Natl. Acad. Sci. USA. 90:1993;7789-7793.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7789-7793
    • Takashima, A.1    Noguchi, K.2    Hoshino, T.3    Imahori, K.4
  • 30
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid β peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β
    • Takashima A., Yamaguchi H., Noguchi K. et al. Exposure of rat hippocampal neurons to amyloid β peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β Neurosci. Lett. 203:1996;33-36.
    • (1996) Neurosci. Lett. , vol.203 , pp. 33-36
    • Takashima, A.1    Yamaguchi, H.2    Noguchi, K.3
  • 32
    • 0027370141 scopus 로고
    • In vivo phosphorylation sites in fetal and adult rat tau
    • Watanabe A., Hasegawa M., Suzuki M. et al. In vivo phosphorylation sites in fetal and adult rat tau. J. Biol. Chem. 268:1993;25712-25717.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25712-25717
    • Watanabe, A.1    Hasegawa, M.2    Suzuki, M.3
  • 33
    • 0029737421 scopus 로고    scopus 로고
    • Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogensynthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II
    • Yamaguchi Y., Ishiguro K., Uchida T., Takashima A., Lemere C.A., Imahori K. Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogensynthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II. Acta Neuropathol. 92:1996;232-241.
    • (1996) Acta Neuropathol. , vol.92 , pp. 232-241
    • Yamaguchi, Y.1    Ishiguro, K.2    Uchida, T.3    Takashima, A.4    Lemere, C.A.5    Imahori, K.6
  • 34
    • 0027340541 scopus 로고
    • Protein kinase Fa/GSK-3 phosphorylates tau on Ser235-Pro and Ser404-Pro that are abnormally phosphorylated in Alzheimer's disease brain
    • Yang S.-D., Song J.-S., Yu J.-S., Shiah S.-G. Protein kinase Fa/GSK-3 phosphorylates tau on Ser235-Pro and Ser404-Pro that are abnormally phosphorylated in Alzheimer's disease brain. J. Neurochem. 61:1993;1742-1747.
    • (1993) J. Neurochem. , vol.61 , pp. 1742-1747
    • Yang, S.-D.1    Song, J.-S.2    Yu, J.-S.3    Shiah, S.-G.4
  • 35
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirshner D.A. Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science. 250:1990;279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirshner, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.